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Jens Christian Jensenius

Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins

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Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. / Holmskov, Uffe Laurits; Laursen, Simon; Malhotra, R; Wiedemann, H; Timpl, R; Stuart, G R; Tornøe, Ida; Madsen, P S; Reid, K B; Jensenius, Jens Christian.

In: Biochemical Journal, Vol. 305 ( Pt 3), 1995, p. 889-96.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Holmskov, UL, Laursen, S, Malhotra, R, Wiedemann, H, Timpl, R, Stuart, GR, Tornøe, I, Madsen, PS, Reid, KB & Jensenius, JC 1995, 'Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins', Biochemical Journal, vol. 305 ( Pt 3), pp. 889-96.

APA

Holmskov, U. L., Laursen, S., Malhotra, R., Wiedemann, H., Timpl, R., Stuart, G. R., Tornøe, I., Madsen, P. S., Reid, K. B., & Jensenius, J. C. (1995). Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Biochemical Journal, 305 ( Pt 3), 889-96.

CBE

Holmskov UL, Laursen S, Malhotra R, Wiedemann H, Timpl R, Stuart GR, Tornøe I, Madsen PS, Reid KB, Jensenius JC. 1995. Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Biochemical Journal. 305 ( Pt 3):889-96.

MLA

Vancouver

Holmskov UL, Laursen S, Malhotra R, Wiedemann H, Timpl R, Stuart GR et al. Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Biochemical Journal. 1995;305 ( Pt 3):889-96.

Author

Holmskov, Uffe Laurits ; Laursen, Simon ; Malhotra, R ; Wiedemann, H ; Timpl, R ; Stuart, G R ; Tornøe, Ida ; Madsen, P S ; Reid, K B ; Jensenius, Jens Christian. / Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. In: Biochemical Journal. 1995 ; Vol. 305 ( Pt 3). pp. 889-96.

Bibtex

@article{c4c2936aa87e4602977995457235e020,
title = "Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins",
abstract = "Collectin-43 (CL-43) is a recently described bovine plasma protein containing both collagenous regions and C-type-lectin domains [Holmskov, Teisner, Willis, Reid and Jensenius (1993) J. Biol. Chem. 268, 10120-10125; Lim, Willis, Reid, Lu, Laursen, Jensenius and Holmskov (1994) J. Biol. Chem. 269, 11820-11824]. CL-43 was purified by affinity chromatography on mannan-Sepharose. On SDS/PAGE under reducing conditions the purified lectin showed a double band at about 43 kDa, with the upper band representing the intact molecule and the lower band a truncated form that lacked the N-terminal nine amino acid residues. Under non-reducing conditions, only one band was seen at 120 kDa. Analytical gel chromatography and sucrose-density-gradient centrifugation of the purified molecule, showed a Stokes radius of 9.1 +/- 0.3 nm (91 +/- 3 A) and a sedimentation coefficient (s20,w) of 3.6 +/- 0.1 S. These values correspond to a molecular mass of 119-138 kDa under non-denaturing condition in solution. The frictional coefficient (f/f0) was 2.7, indicating extreme elongation due to the collagenous segment. Only monomer subunits, with 37.4 +/- 1.7-nm-long rods, were seen by electron microscopy. These findings indicate that CL-43, in contrast with the other circulating collectins, is found only as a single subunit composed of three polypeptide chains. Two-dimensional gel electrophoresis showed that CL-43 has two isoforms, with pI values of 4.9 and 5.3, corresponding to the native form and the truncated form of the molecule respectively. CL-43, like conglutinin, lung surfactant protein A and mannan-binding protein (MBP), was shown to bind to the collectin receptor. Bovine MBP caused the activation of the complement system as revealed by the deposition of complement component C4 upon incubation of diluted serum in wells containing MBP bound to solid-phase mannan. CL-43, lung surfactant protein D (SP-D) and conglutinin showed no complement-activating properties under the same conditions. Conglutinin binds fluid- and solid-phase iC3b, while CL-43 and MBP do not show such reactivity.",
keywords = "Animals, Carrier Proteins, Cattle, Centrifugation, Density Gradient, Chemistry, Physical, Chromatography, Chromatography, Affinity, Collectins, Complement Activation, Complement C3b, Electrophoresis, Gel, Two-Dimensional, Isoelectric Point, Lectins, Microscopy, Electron, Molecular Weight, Physicochemical Phenomena, Proteolipids, Pulmonary Surfactant-Associated Proteins, Pulmonary Surfactants, Receptors, Cell Surface, Serum Globulins",
author = "Holmskov, {Uffe Laurits} and Simon Laursen and R Malhotra and H Wiedemann and R Timpl and Stuart, {G R} and Ida Torn{\o}e and Madsen, {P S} and Reid, {K B} and Jensenius, {Jens Christian}",
year = "1995",
language = "English",
volume = "305 ( Pt 3)",
pages = "889--96",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",

}

RIS

TY - JOUR

T1 - Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins

AU - Holmskov, Uffe Laurits

AU - Laursen, Simon

AU - Malhotra, R

AU - Wiedemann, H

AU - Timpl, R

AU - Stuart, G R

AU - Tornøe, Ida

AU - Madsen, P S

AU - Reid, K B

AU - Jensenius, Jens Christian

PY - 1995

Y1 - 1995

N2 - Collectin-43 (CL-43) is a recently described bovine plasma protein containing both collagenous regions and C-type-lectin domains [Holmskov, Teisner, Willis, Reid and Jensenius (1993) J. Biol. Chem. 268, 10120-10125; Lim, Willis, Reid, Lu, Laursen, Jensenius and Holmskov (1994) J. Biol. Chem. 269, 11820-11824]. CL-43 was purified by affinity chromatography on mannan-Sepharose. On SDS/PAGE under reducing conditions the purified lectin showed a double band at about 43 kDa, with the upper band representing the intact molecule and the lower band a truncated form that lacked the N-terminal nine amino acid residues. Under non-reducing conditions, only one band was seen at 120 kDa. Analytical gel chromatography and sucrose-density-gradient centrifugation of the purified molecule, showed a Stokes radius of 9.1 +/- 0.3 nm (91 +/- 3 A) and a sedimentation coefficient (s20,w) of 3.6 +/- 0.1 S. These values correspond to a molecular mass of 119-138 kDa under non-denaturing condition in solution. The frictional coefficient (f/f0) was 2.7, indicating extreme elongation due to the collagenous segment. Only monomer subunits, with 37.4 +/- 1.7-nm-long rods, were seen by electron microscopy. These findings indicate that CL-43, in contrast with the other circulating collectins, is found only as a single subunit composed of three polypeptide chains. Two-dimensional gel electrophoresis showed that CL-43 has two isoforms, with pI values of 4.9 and 5.3, corresponding to the native form and the truncated form of the molecule respectively. CL-43, like conglutinin, lung surfactant protein A and mannan-binding protein (MBP), was shown to bind to the collectin receptor. Bovine MBP caused the activation of the complement system as revealed by the deposition of complement component C4 upon incubation of diluted serum in wells containing MBP bound to solid-phase mannan. CL-43, lung surfactant protein D (SP-D) and conglutinin showed no complement-activating properties under the same conditions. Conglutinin binds fluid- and solid-phase iC3b, while CL-43 and MBP do not show such reactivity.

AB - Collectin-43 (CL-43) is a recently described bovine plasma protein containing both collagenous regions and C-type-lectin domains [Holmskov, Teisner, Willis, Reid and Jensenius (1993) J. Biol. Chem. 268, 10120-10125; Lim, Willis, Reid, Lu, Laursen, Jensenius and Holmskov (1994) J. Biol. Chem. 269, 11820-11824]. CL-43 was purified by affinity chromatography on mannan-Sepharose. On SDS/PAGE under reducing conditions the purified lectin showed a double band at about 43 kDa, with the upper band representing the intact molecule and the lower band a truncated form that lacked the N-terminal nine amino acid residues. Under non-reducing conditions, only one band was seen at 120 kDa. Analytical gel chromatography and sucrose-density-gradient centrifugation of the purified molecule, showed a Stokes radius of 9.1 +/- 0.3 nm (91 +/- 3 A) and a sedimentation coefficient (s20,w) of 3.6 +/- 0.1 S. These values correspond to a molecular mass of 119-138 kDa under non-denaturing condition in solution. The frictional coefficient (f/f0) was 2.7, indicating extreme elongation due to the collagenous segment. Only monomer subunits, with 37.4 +/- 1.7-nm-long rods, were seen by electron microscopy. These findings indicate that CL-43, in contrast with the other circulating collectins, is found only as a single subunit composed of three polypeptide chains. Two-dimensional gel electrophoresis showed that CL-43 has two isoforms, with pI values of 4.9 and 5.3, corresponding to the native form and the truncated form of the molecule respectively. CL-43, like conglutinin, lung surfactant protein A and mannan-binding protein (MBP), was shown to bind to the collectin receptor. Bovine MBP caused the activation of the complement system as revealed by the deposition of complement component C4 upon incubation of diluted serum in wells containing MBP bound to solid-phase mannan. CL-43, lung surfactant protein D (SP-D) and conglutinin showed no complement-activating properties under the same conditions. Conglutinin binds fluid- and solid-phase iC3b, while CL-43 and MBP do not show such reactivity.

KW - Animals

KW - Carrier Proteins

KW - Cattle

KW - Centrifugation, Density Gradient

KW - Chemistry, Physical

KW - Chromatography

KW - Chromatography, Affinity

KW - Collectins

KW - Complement Activation

KW - Complement C3b

KW - Electrophoresis, Gel, Two-Dimensional

KW - Isoelectric Point

KW - Lectins

KW - Microscopy, Electron

KW - Molecular Weight

KW - Physicochemical Phenomena

KW - Proteolipids

KW - Pulmonary Surfactant-Associated Proteins

KW - Pulmonary Surfactants

KW - Receptors, Cell Surface

KW - Serum Globulins

M3 - Journal article

C2 - 7848290

VL - 305 ( Pt 3)

SP - 889

EP - 896

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

ER -